Energy transfer from tryptophan residues of proteins to 8-anilinonaphthalene-1-sulfonate View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-10

AUTHORS

Long-sen Chang, Ehr-ya Wen, Jen-jung Hung, Chung-chang Chang

ABSTRACT

The binding of the apolar fluorescent dye 8-anilinonaphthalene-1-sulfonate (ANS) to bovine serum albumin (BSA), phospholipase A2 (PLA2), ovalbumin, lysozyme, cobrotoxin and N-acetyltryptophanamide was used to assess the factors affecting the efficiency of energy transfer from Trp residues to the ANS molecule. We found that the efficiency of energy transfer from Trp residues to ANS was associated with the ability of proteins to enhance the ANS fluorescence. At the same molar concentration of protein, BSA enhanced ANS fluorescence most among these proteins; its Trp fluorescence was drastically quenched by the addition of ANS. Fluorescence enhancement of ANS in PLA2-ANS complex increased upon addition of Ca2+ or change of the buffer to acidicpH, resulting in a higher efficiency of energy transfer from Trp residues to ANS. There was limited ANS fluorescence enhancement with ovalbumin, lysozyme, cobrotoxin, and N-acetyltryptophanamide and a less efficient quenching in Trp fluorescence. The capabilities of proteins for binding with ANS correlated with the decrease in their Trp fluorescence being quenching by ANS. However, the microenvironment surrounding Trp residues of proteins did not affect the energy transfer. Based on these results, the factors that affected the energy transfer from Trp residues to ANS are discussed. More... »

PAGES

635-640

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01890462

DOI

http://dx.doi.org/10.1007/bf01890462

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042689728

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7702745


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